DOSC_SHIBS
ID DOSC_SHIBS Reviewed; 460 AA.
AC Q320T0; Q320S9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Diguanylate cyclase DosC;
DE Short=DGC;
DE EC=2.7.7.65;
DE AltName: Full=Direct oxygen-sensing cyclase;
GN Name=dosC; OrderedLocusNames=SBO_1566/SBO_1567;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Globin-coupled heme-based oxygen sensor protein displaying
CC diguanylate cyclase (DGC) activity in response to oxygen availability.
CC Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the
CC condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger
CC which controls cell surface-associated traits in bacteria (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate;
CC Xref=Rhea:RHEA:24898, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:58805; EC=2.7.7.65;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
CC -!- DOMAIN: Is composed of an N-terminal sensory globin-fold domain that
CC binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase
CC domain. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB66178.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABB66179.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000036; ABB66178.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000036; ABB66179.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q320T0; -.
DR SMR; Q320T0; -.
DR EnsemblBacteria; ABB66178; ABB66178; SBO_1566.
DR EnsemblBacteria; ABB66179; ABB66179; SBO_1567.
DR KEGG; sbo:SBO_1566; -.
DR KEGG; sbo:SBO_1567; -.
DR HOGENOM; CLU_1155769_0_0_6; -.
DR UniPathway; UPA00599; -.
DR Proteomes; UP000007067; Chromosome.
DR GO; GO:0052621; F:diguanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd14757; GS_EcDosC-like_GGDEF; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR039435; DosC_GS.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR044398; Globin-sensor_dom.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF11563; Protoglobin; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR TIGRFAMs; TIGR00254; GGDEF; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 3: Inferred from homology;
KW GTP-binding; Heme; Iron; Magnesium; Metal-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..460
FT /note="Diguanylate cyclase DosC"
FT /id="PRO_0000316154"
FT DOMAIN 325..458
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 98
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 43
FT /note="Involved in oxygen binding and important for the
FT stability of the Fe(II)-O(2) complex"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Important for oxygen binding and stability of the
FT Fe(II)-O(2) complex"
FT /evidence="ECO:0000250"
FT SITE 65
FT /note="Critical for restricting water access to the heme
FT distal side to avoid rapid autoxidation"
FT /evidence="ECO:0000250"
FT SITE 338
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 53194 MW; 7A34AA1B3E5E24DF CRC64;
MEMYFKRMKD EWTGLVEQAD PLIRAKAAEI AVAHAHYLSI EFYRIVRIDP HAEEFLSNEQ
VERQLKSAME RWIINVLSAQ VDDVERLIQI QHTVAEVHAR IGIPVEIVEM GFRVLKKILY
PVIFSSDYSA AEKLQVYHFS INSIDIAMEV MTRAFTFSDS SASKEDENYR IFSLLENAEE
EKERQIASIL SWEIDIIYKI LLDSDLGSSL PLSQADFGLW FNHKGRHYFS GIAEVGHISR
LIQDFDGIFN QTMRNTRNLN NRSLRVKFLL QIRNTVSQII TLLRELFEEV SRHEVGMDVL
TKLLNRRFLP TIFKREIAHA NRTGTPLSVL IIDVDKFKEI NDTWGHNTGD EILRKVSQAF
YDNVRSSDYV FRYGGDEFII VLTEASENET LRTAERIRSR VEKTKLKAAN GEDIALSLSI
GAAMFNGHPD YERLIQIADE ALYIAKRRGR NRVELWKASL
